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- Gordon, E.H.J., Sjögren, T., Löfqvist, M., Richter, C.D., Allen, J.W.A., Higham, C.W., Hajdu, J., Fülöp, V., Ferguson, S.J.
(author)
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Structure and Kinetic Properties of Paracoccus pantotrophus Cytochrome cd1 Nitrite Reductase with the d1 Heme Active Site Ligand Tyrosine 25 Replaced by Serine.
- 2003
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In: J. Biol. Chem.. ; 278, s. 11773-11781
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Journal article (peer-reviewed)
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- Hajdu, J, et al.
(author)
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Analyzing protein functions in four dimensions
- 2000
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In: NATURE STRUCTURAL BIOLOGY. - : NATURE AMERICA INC. ; 7:11, s. 1006-1012
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Review (other academic/artistic)abstract
- Time-resolved structural studies on biomolecular function are coming of age. Focus has shifted from studies on 'systems of opportunities' to a more problem-oriented approach, addressing significant questions in biology and chemistry. An important step in
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- Hajdu, J
(author)
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Single-molecule X-ray diffraction
- 2000
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In: CURRENT OPINION IN STRUCTURAL BIOLOGY. - : CURRENT BIOLOGY LTD. - 0959-440X. ; 10:5, s. 569-573
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Journal article (peer-reviewed)abstract
- Free-electron lasers could provide femtosecond X-ray flashes with a peak brilliance 10-11 orders of magnitude higher than that which is currently available from synchrotrons. Such pulses may allow structural studies of single biomolecules before radiation
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- Neutze, R, et al.
(author)
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Potential for biomolecular imaging with femtosecond X-ray pulses
- 2000
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In: NATURE. - 0028-0836. ; 406:6797, s. 752-757
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Journal article (peer-reviewed)abstract
- Sample damage by X-rays and other radiation limits the resolution of structural studies on non-repetitive and non-reproducible structures such as individual biomolecules or cells(1). Cooling can slow sample deterioration, but cannot eliminate damage-induc
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12. |
- Sjogren, T, et al.
(author)
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The structure of an alternative form of Paracoccus pantotrophus cytochrome cd(1) nitrite reductase
- 2001
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In: JOURNAL OF BIOLOGICAL CHEMISTRY. - : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC. - 0021-9258. ; 276:31, s. 29450-29455
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Journal article (peer-reviewed)abstract
- Cytochrome ed(1) nitrite reductase is a bifunctional enzyme, which can catalyze the I-electron reduction of nitrite to nitric oxide and the 4-electron reduction of dioxygen to water. Here we describe the structure of reduced nitrite reductase, crystallize
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16. |
- Wilmouth, RC, et al.
(author)
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X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate
- 2001
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In: NATURE STRUCTURAL BIOLOGY. - : NATURE AMERICA INC. - 1072-8368. ; 8:8, s. 689-694
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Journal article (peer-reviewed)abstract
- Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed b
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